Binary ionic porphyrin nanosheets: electronic and light-harvesting properties regulated by crystal structure

Nanoscale ◽  
2012 ◽  
Vol 4 (5) ◽  
pp. 1695 ◽  
Author(s):  
Yongming Tian ◽  
Christine M. Beavers ◽  
Tito Busani ◽  
Kathleen E. Martin ◽  
John L. Jacobsen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Light Harvesting

Crystal Structure of Archaeal Photolyase from Sulfolobus tokodaii with Two FAD Molecules: Implication of a Novel Light-harvesting Cofactor

2007 ◽  
Vol 365 (4) ◽  
pp. 903-910 ◽  
Author(s):  
Masahiro Fujihashi ◽  
Nobutaka Numoto ◽  
Yukiko Kobayashi ◽  
Akira Mizushima ◽  
Masanari Tsujimura ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Light Harvesting ◽  
Sulfolobus Tokodaii

scholarly journals The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore

2015 ◽  
Vol 112 (52) ◽  
pp. 15880-15885 ◽  
Author(s):  
Kun Tang ◽  
Wen-Long Ding ◽  
Astrid Höppner ◽  
Cheng Zhao ◽  
Lun Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transient Absorption ◽  
Light Harvesting ◽  
Reaction Centers ◽  
Protein Fold ◽  
Light Harvesting Complexes ◽  
Exciton Coupling ◽  
Femtosecond Transient Absorption ◽  
Orange Carotenoid Protein ◽  
Sensory Photoreceptors

Photosynthesis relies on energy transfer from light-harvesting complexes to reaction centers. Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, attach to the membrane via the multidomain core-membrane linker, LCM. The chromophore domain of LCM forms a bottleneck for funneling the harvested energy either productively to reaction centers or, in case of light overload, to quenchers like orange carotenoid protein (OCP) that prevent photodamage. The crystal structure of the solubly modified chromophore domain from Nostoc sp. PCC7120 was resolved at 2.2 Å. Although its protein fold is similar to the protein folds of phycobiliproteins, the phycocyanobilin (PCB) chromophore adopts ZZZssa geometry, which is unknown among phycobiliproteins but characteristic for sensory photoreceptors (phytochromes and cyanobacteriochromes). However, chromophore photoisomerization is inhibited in LCM by tight packing. The ZZZssa geometry of the chromophore and π-π stacking with a neighboring Trp account for the functionally relevant extreme spectral red shift of LCM. Exciton coupling is excluded by the large distance between two PCBs in a homodimer and by preservation of the spectral features in monomers. The structure also indicates a distinct flexibility that could be involved in quenching. The conclusions from the crystal structure are supported by femtosecond transient absorption spectra in solution.

scholarly journals Uncovering dark multichromophoric states in Peridinin–Chlorophyll–Protein

2020 ◽  
Vol 17 (164) ◽  
pp. 20190736
Author(s):  
Elliot J. Taffet ◽  
Francesca Fassioli ◽  
Zi S. D. Toa ◽  
David Beljonne ◽  
Gregory D. Scholes
Keyword(s):  
Crystal Structure ◽  
Excited States ◽  
Quantum Chemical ◽  
Light Harvesting ◽  
Singlet Fission ◽  
Chlorophyll Protein ◽  
Triplet Pair ◽  
A Charge ◽  
Hole Generation ◽  
Chemical Evidence

It has long been recognized that visible light harvesting in Peridinin–Chlorophyll–Protein is driven by the interplay between the bright (S 2 ) and dark (S 1 ) states of peridinin (carotenoid), along with the lowest-lying bright (Q y ) and dark (Q x ) states of chlorophyll- a . Here, we analyse a chromophore cluster in the crystal structure of Peridinin–Chlorophyll–Protein, in particular, a peridinin–peridinin and a peridinin–chlorophyll- a dimer, and present quantum chemical evidence for excited states that exist beyond the confines of single peridinin and chlorophyll chromophores. These dark multichromophoric states, emanating from the intermolecular packing native to Peridinin–Chlorophyll–Protein, include a correlated triplet pair comprising neighbouring peridinin excitations and a charge-transfer interaction between peridinin and the adjacent chlorophyll- a . We surmise that such dark multichromophoric states may explain two spectral mysteries in light-harvesting pigments: the sub-200-fs singlet fission observed in carotenoid aggregates, and the sub-200-fs chlorophyll- a hole generation in Peridinin–Chlorophyll–Protein.

Crystal Structure of a Light-Harvesting Protein C-Phycocyanin from Spirulina platensis

2001 ◽  
Vol 282 (4) ◽  
pp. 893-898 ◽  
Author(s):  
Anil K. Padyana ◽  
Vadiraja B. Bhat ◽  
K.M. Madyastha ◽  
K.R. Rajashankar ◽  
S. Ramakumar
Keyword(s):  
Crystal Structure ◽  
Spirulina Platensis ◽  
Protein C ◽  
Light Harvesting

scholarly journals Crystal Structure of a Multilayer Packed Major Light-Harvesting Complex: Implications for Grana Stacking in Higher Plants

2014 ◽  
Vol 7 (5) ◽  
pp. 916-919 ◽  
Author(s):  
Tao Wan ◽  
Mei Li ◽  
Xuelin Zhao ◽  
Jiping Zhang ◽  
Zhenfeng Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Light Harvesting ◽  
Higher Plants ◽  
Light Harvesting Complex

scholarly journals Crystal structure of plant light-harvesting complex shows the active, energy-transmitting state

2009 ◽  
Vol 28 (3) ◽  
pp. 298-306 ◽  
Author(s):  
Tiago Barros ◽  
Antoine Royant ◽  
Jörg Standfuss ◽  
Andreas Dreuw ◽  
Werner Kühlbrandt
Keyword(s):  
Crystal Structure ◽  
Light Harvesting ◽  
Light Harvesting Complex
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